Haemoglobin unfolding studies at the liquid-liquid interface
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The electrochemical behaviour of haemoglobin denatured using different concentrations of urea was investigated at the liquid|liquid interface. The reverse peak current varied with the concentration of urea, allowing the building of the unfolding curve, which compares well with UV-Vis absorbance results. Thermodynamic parameters, such as the change in free energy of folding in water, , and the index of the compactness of the protein, m, were extracted from the experimental data. The work here presents a simple electrochemical method for the study of protein unfolding by electrochemistry at the liquid | liquid interface.
NOTICE: This is the author's version of a work that was accepted for publication in Electrochemistry Communications. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Electrochemistry Communications, 13, 7, 2011. DOI: 10.1016/j.elecom.2011.04.020
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